<p>The difficulty of obtaining collagen peptides from connective tissues is due to the high mechanical strength of collagen fibrils. Collagen hydrolysates were obtained after ultrasonic homogenization of hyaline cartilages. Homogenization was performed at temperatures denaturing collagen and under conditions of enzymatic hydrolysis. The particle sizes were determined by photon correlation spectroscopy. According to spectral studies, the particles in the samples obtained at a karipazim concentration of 10% have the smallest size. Karipazim at a concentration of 10% is preferred for the enzymatic hydrolysis of hyaline cartilage and the production of low-molecular-weight type II collagen peptides. The peptides were distributed in the range from 180 to 600 Da. Collagen peptides containing two to five amino-acid residues are convenient in size for use in biomedicine.</p>

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Collagen Peptides Made of Pork Hyaline Cartilages for Nutritiology and Biomedicine

  • T. I. Nikolaeva,
  • T. N. Pachovkin,
  • E. V. Grishina,
  • K. S. Laurinavichu,
  • P. V. Shekhovtsov

摘要

The difficulty of obtaining collagen peptides from connective tissues is due to the high mechanical strength of collagen fibrils. Collagen hydrolysates were obtained after ultrasonic homogenization of hyaline cartilages. Homogenization was performed at temperatures denaturing collagen and under conditions of enzymatic hydrolysis. The particle sizes were determined by photon correlation spectroscopy. According to spectral studies, the particles in the samples obtained at a karipazim concentration of 10% have the smallest size. Karipazim at a concentration of 10% is preferred for the enzymatic hydrolysis of hyaline cartilage and the production of low-molecular-weight type II collagen peptides. The peptides were distributed in the range from 180 to 600 Da. Collagen peptides containing two to five amino-acid residues are convenient in size for use in biomedicine.